Laura Molina

 Laura Molina
Mentor: Dr. Alexander Angerhofer
College of Liberal Arts and Sciences
 
"I have always been interested in biochemistry and molecular biology, and I hope to pursue a career in biomedical research by attending an MD/PhD program. By participating in the University Scholars Program, I hope to join a community of scholars who are passionate about conducting research and expanding their knowledge of their field while gaining professional experience that will prove invaluable in graduate/professional school. Working with Professor Alexander Angerhofer for the past year has broadened my horizons both intellectually and professionally, and has given me the opportunity to apply what I have learned in my classes to a real-world biochemical problem. I look forward to continuing this learning experience next year and making a contribution to my field."

Major

Biochemistry

Minor

Art History, French

Research Interests

  • Biochemistry
  • Enzyme Catalysis
  • Electron Paramagnetic Resonance for Biological Applications

Academic Awards

  • National Merit Scholar
  • UF CLAS Dean's List and UF President's Honor Roll
  • Bright Futures Academic Top Scholar
  • College Board National AP Scholar

Organizations

  • Phi Beta Kappa
  • BCH 4024 Supplemental Instruction Program, private tutor
  • UF Honors Program

Volunteer

  • Malcolm Randall VA Hospital
  • Viera VA Outpatient Clinic
  • Undergraduate Researcher in UF Chemistry Department

Hobbies and Interests

  • Foreign languages (French, German)
  • Traveling
  • Classic Literature
  • European Paintings, 15th to 19th Century

Research Description

Elucidation of the Catalytic Mechanism of Oxalate Decarboxylase using Pulsed-EPR Techniques
Oxalate decarboxylase (OxDC), a bicupin enzyme isolated from Bacillus subtilis, catalyzes the decomposition of oxalate, a major human dietary toxin, into carbon dioxide and formate in the presence of oxygen. OxDC uses Mn(II) to catalyze the breakdown of oxalate. Although two Mn atoms must be bound to each enzyme subunit for the reaction to take place, evidence suggests that only the N-terminal Mn atom binds substrate. This leaves in question the role of the C-terminal Mn, which could serve as a binding site for molecular oxygen. My research will focus on studying the binding of OxDC inhibitors and analogs of molecular oxygen using electron paramagnetic resonance spectroscopy (EPR), especially pulsed-EPR techniques at X-band such as ESEEM (electron spin echo envelope modulation). In EPR experiments, paramagnetic species, such as the Mn centers and radical reaction intermediates, are placed in an external variable magnetic field and are detected using microwave radiation at a fixed frequency. These experiments should provide significant insights into the catalytic mechanism of OxDC and pave the way for the use of OxDC in the breakdown of oxalate for therapeutic and industrial purposes.